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REVIEW: Role of Glyceraldehyde-3-phosphate Dehydrogenase in Vesicular Transport from Golgi Apparatus to Endoplasmic Reticulum

A. V. Bryksin* and P. P. Laktionov

Institute of Chemical Biology and Fundamental Medicine, pr. Akademika Lavrent'eva 8, 630090 Novosibirsk, Russia; E-mail: anton.bryksin@gmail.com

* To whom correspondence should be addressed.

Received August 10, 2007; Revision received October 4, 2007
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a well-studied glycolytic protein with energy production as its implied occupation. It has established itself lately as a multifunctional protein. Recent studies have found GAPDH to be involved in a variety of nuclear and cytosolic pathways ranging from its role in apoptosis and regulation of gene expression to its involvement in regulation of Ca2+ influx from endoplasmic reticulum. Numerous studies also indicate that GAPDH interacts with microtubules and participates in cell membrane fusion. This review is focused on the cytosolic functions of the protein related to vesicular transport. Suggestions for future directions as well as the model of protein polymer structure and possible post-translational modifications as a basis for its multifunctional activities in the early secretory pathway are given.
KEY WORDS: glyceraldehyde-3-phosphate dehydrogenase, microtubules, phosphorylation, membranes, vesicles, Golgi apparatus, endoplasmic reticulum, COPI, COPII

DOI: 10.1134/S0006297908060011